ID F8QSY0_9EUKA Unreviewed; 1057 AA.
AC F8QSY0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
DE Flags: Fragment;
GN Name=Rpb1 {ECO:0000313|EMBL:AEA40840.1};
OS Trichomitus batrachorum.
OC Eukaryota; Metamonada; Parabasalia; Hypotrichomonadida;
OC Hypotrichomonadidae; Trichomitus.
OX NCBI_TaxID=5732 {ECO:0000313|EMBL:AEA40840.1};
RN [1] {ECO:0000313|EMBL:AEA40840.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G11 {ECO:0000313|EMBL:AEA40840.1};
RA Malik S.-B., Brochu C.D., Bilic I., Yuan J., Hess M., Logsdon J.M.Jr.,
RA Carlton J.M.;
RT "Phylogeny of Parasitic Parabasalia and Free-Living Relatives Inferred from
RT Conventional Markers vs. Rpb1, a Single-Copy Gene.";
RL PLoS ONE 6:E20774-E20774(2011).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|RuleBase:RU004279}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00024550,
CC ECO:0000256|RuleBase:RU004279};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; HM016232; AEA40840.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QSY0; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 180..482
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 73..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEA40840.1"
FT NON_TER 1057
FT /evidence="ECO:0000313|EMBL:AEA40840.1"
SQ SEQUENCE 1057 AA; 118362 MW; A66E38DF985FC9E7 CRC64;
HIKLATVLYH IGYIDIVYKI LQCVCPSCSR LLVGYADPHV QEAVLRYKGK KRLLAIHAIA
TKSSTRYCKH LEKKKSTKGV SGPNQAQQSN PEEADYVKND RFWKIVTGSD DQEKWKRESQ
PCGNAVPELT KENDGHIKKK DPARGEPDLI ESSKVLEILH NISEQDIRIL GFDPQKCRPE
WMMVKILPVP PPHVRPFIRQ GGHVTQDEVS HQLGQIILLN KKVQEDITNG IPATKRQEDE
FALQQCVTTY FINDKPSIDR ATLKNGRPIK AISQRLKGKM GHIRGHLSGK RVNFSARSVI
SPDPSISIDQ VGVPFELAKI LTFPEVVNSL NIKDMQQLVY NGPDSQDGAK AVITPLGARF
SLGDTQESTV QHLDYGSVVE RHLRDNDIVI FNRQPSLHKM SMMGHYAKLI RGQSFRLNLC
VTTPYNADFD GDEMNLHVVQ TQQARAEVKH IMAVPYQIIT PQSNKPIIGL VQDCLVGCRL
LSIRDTFLTR NELMNLMMWI MDTKPDLVLP PPCIVAPQEL WSGKQVFSLF LPQINLDKFS
SPADDKGADK SWNSSDDVRV IIRDGHLLAG IIDSKTVAKS EGSLTHVVIN SYSLDTAKAF
LNQTQLVVNN WLENRGFSMG ISTCVTTQEA LDKVAGQLTE LKAKIETIIE DAKHDRLEKM
PGLTLTGTFE AKIMEVANDF TEKSSAVAIQ AAPFWNALLQ MMQAGSKGSK VNIAQIIACV
GQQSIEGERV RFGFKNRTLP HYVKDDFDLE SRGFVEHSYI QGLTPQEFFF HSMGGRTGII
DTACKTADTG YIQRRLCKTM ESHCVQYDGT VRDSMNNVVQ FLYGGDGIDP VQIETQSLSL
IALSDQEFDS MYKMNINDPV FGAGYLESSI ISDLRKMEGT PTTTITGNFG GRSEEVEITR
PSAVLQEELD TLLHFRQILR EEIFPNGNQK LYASVNLKRI IETAQRKYNI NEYTSLSDLN
PVLVVSEVKK LVSRLIIVQQ NKDKIGREVQ DNGTLLLRIL IHATLASKPL IEKNRLSQKA
FRSIIGEIED RFYRTIVSPG EMVGTIAGQS IGEPATQ
//
